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Article

A chaperonin subunit with unique structures is essential for folding of a specific substrate.

PLoS biology - 1 Apr 2011

Peng Lianwei, Fukao Yoichiro, Myouga Fumiyoshi, Motohashi Reiko, Shinozaki Kazuo, Shikanai Toshiharu

Abstract excerpt

Type I chaperonins are large, double-ring complexes present in bacteria (GroEL), mitochondria (Hsp60), and chloroplasts (Cpn60), which are involved in mediating the folding of newly synthesized, translocated, or stress-denatured proteins. In Escherichia coli, GroEL comprises 14 identical subunits and has been exquisitely optimized to fold its broad range of substrates. However, multiple Cpn60 subunits with...

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Source

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Identifiers

PMID: 21483722
DOI: 10.1371/journal.pbio.1001040
PMCID: PMC3071376

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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